ID   A1KQY6_RAT              Unreviewed;       454 AA.
AC   A1KQY6; F1MA57;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4 {ECO:0000313|Ensembl:ENSRNOP00000026010.5};
GN   Name=St8sia4 {ECO:0000313|Ensembl:ENSRNOP00000026010.5,
GN   ECO:0000313|RGD:621845};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000026010.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000026010.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026010.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000026010.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026010.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000256|ARBA:ARBA00006003}.
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DR   RefSeq; NP_446366.1; NM_053914.1.
DR   AlphaFoldDB; A1KQY6; -.
DR   SMR; A1KQY6; -.
DR   STRING; 10116.ENSRNOP00000026010; -.
DR   PaxDb; 10116-ENSRNOP00000026010; -.
DR   Ensembl; ENSRNOT00000026010.7; ENSRNOP00000026010.5; ENSRNOG00000019128.7.
DR   GeneID; 116696; -.
DR   KEGG; rno:116696; -.
DR   AGR; RGD:621845; -.
DR   CTD; 7903; -.
DR   RGD; 621845; St8sia4.
DR   eggNOG; KOG2692; Eukaryota.
DR   GeneTree; ENSGT01030000234535; -.
DR   HOGENOM; CLU_048583_3_0_1; -.
DR   OMA; HAAEGWK; -.
DR   OrthoDB; 5348004at2759; -.
DR   Reactome; R-RNO-4085001; Sialic acid metabolism.
DR   Reactome; R-RNO-419037; NCAM1 interactions.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000019128; Expressed in spleen and 18 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; ISO:RGD.
DR   GO; GO:0008373; F:sialyltransferase activity; TAS:RGD.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; ISO:RGD.
DR   GO; GO:0006491; P:N-glycan processing; ISO:RGD.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; TAS:RGD.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; ISO:RGD.
DR   GO; GO:0006486; P:protein glycosylation; ISO:RGD.
DR   GO; GO:0097503; P:sialylation; ISO:RGD.
DR   Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   PANTHER; PTHR11987; ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR11987:SF48; CMP-N-ACETYLNEURAMINATE-POLY-ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  51762 MW;  4644DA8D857E7D36 CRC64;
     MHKVSHLKRN PSPREAAQSD PSPASANCAA GRWAALENRE SSTAERPSDL ILGSRLHAPF
     ANFRFLPLDY FPKTEPLYQE KVPELGQPGL SRAPKMRSIR KRWTICTISL LLIFYKTKEI
     ARTEEHQETQ LIGDGELCLS RSLVNNSDKI TRKAGSTIFQ HSVQGWKINS SLVLEIRKNI
     LRFLDAERDV SVVKSSFKPG DVIHYVLDRR RTLNISHDLH SLLPEVSPMK NRRFKTCAVV
     GNSGILLDSG CGKEIDSHNF VIRCNLAPVV EFAADVGTKS DFITMNPSVV QRAFGGFRNE
     SDREKFVHRL SMLNDSVLWI PAFMVKGGEK HVEWVNALIL KNKLKVRTAY PSLRLIHAVR
     GYWLTNKVPI KRPSTGLLMY TLATRFCDEI HLYGFWPFPK DLNGKAVKYH YYDDLKYRYF
     SNASPHRMPL EFKTLNVLHN RGALKLTTGK CMKQ
//